1. CARBOHYDRATES
2. LIPIDS
3. PROTEIN
4. NUCLEIC ACID
BIOMOLECULES
Biomolecules are the chemical compound found in living organism, involved
in the maintenance and metabolic process of living organism.
Cells are basic structural and functional units of living organisms, are highly organized and constant
source of energy, required to maintain the life.
Biochemical organization of Cell: Atoms are organized into molecules, molecules into organelles,
organelles into cells, cell organized to form tissue, tissue organized to form organ, organ to organ
system and organ system organized to form organism.
Biomolecules are defined as any organic molecule present in a living cell. Biomolecules are
mainly composed of major six elements, carbon, hydrogen, oxygen and nitrogen, sulphur and
phosphorus. The next major elements are sodium, chlorine, potassium, calcium and magnesium.
These make up to 3-5 % of living thing. Trace elements present at low level (1%) of living cell
includes iron, iodine, manganese, molybdenum, selenium, silicon, tin, vanadium, boron, chromium,
cobalt, copper and fluorine.
Each Biomolecules is essential for body functions. They have wide range of size, structure and
perform various types of function.
The four major types of Biomolecules are:
Organized to form
Ft inisgelluingre1: Biochemical organization of cell
Major elements (95-97 %)
C, H, O, N
Bioelements
Trace element (1%)
(Fe, Cu, Zn, Mo, B, Mn)
Minor elements (3-5 %)
Na, K, Ca, S, P, Cl, Mg
MICRO MOLECULE
1. Water
2. Mineral
3. Monosaccharide
4. Disaccharide
5. Fatty acid
6. Amino acid
7. Nucleotide
BIOMOLECULES
MACRO MOLECULE
1. Polysaccharide(Carbohydrate)
2. Protein
3. Fat/Lipid
4. Nucleic acid
Cell organelles and
Cytoplasm
Tissue
Organ
Organ system
Organism
Cell
MONOSACCHARIDES OLIGOSACCHARIDES
Contain only one sugar molecule
Aldoses
Polymers of monosaccharide contain
2-10 sugar units (molecules)
Tetrasaccharide
E.g Stachyose
(Glucose + Fructose +
Galactose + Galactose)
Yield two
monosaccharide
on hydrolysis
E.g. Maltose
(Glucose + Glucose),
Sucrose
(Glucose + Fructose)
E.g. Raffinose
(Glucose + Fructose +
Galactose)
Homo polysaccharide
Long chain polymer of monosaccharide
either straight chain or branched
POLYSACCHARIDES
Hetero polysaccharide
Ketoses Yield three
monosaccharide
on hydrolysis
Yield four
monosaccharide
on hydrolysis
Disaccharide Trisaccharide
CLASSIFICATION OF PROTEIN
(Physical and chemical nature)
E.g. Starch, Glycogen,
Cellulose
Non sweet and insoluble in water.
Donot Reduce Fehling and Benedict reagent.
Cannot be hydrolyzed
E.g. Galactose
Ribose, Glucose
Contain Aldehyde
E.g. Ribulose,
Fructose
Contain Ketone
CLASSIFICATION OF CARBOHYDRATE
(CHEMICAL NATURE)
On hydrolysis gives
single
monosaccharide unit
E.g. Starch, Glycogen
On hydrolysis gives
multiple
monosaccharide unit
E.g. Hyaluronic acid
NON SUGARSUGAR
Reducing sugar
Sweet and soluble in water.
Reduce Fehling and
Benedict reagent.
E.g. Glucose, Fructose,
Lactose, Maltose
Non reducing sugar
Sweet and soluble in water.
Donot Reduce Fehling and
Benedict reagent.
E.g. Sucrose
INTRODUCTION
The proteins are most abundant macro molecules in the cells and they constitute over half the dry
weight of most of the organism. They are made up of 20 standard a-amino acids. They are
mainly composed of C, H, O, N elements. Some proteins also contain S, P element also.
Chemically proteins are polymers of L-α-amino acids. Amino acids are polymerized through
formation of number of peptide linkages. Protein molecule consists of very long chains having
about 100-1000 amino acids unit joined by Peptide linkages. Cell contains 100 or 1000 of
different protein, each with different function and biological activity.
Proteins are nitrogenous organic compounds of high molecular weight which play a
vital or prime role in living organisms.
PROPERTIES OF PROTEIN
1. Solubility: Form colloidal solution in water
2. Molecular weight: Majority of amino acid consist of 40-4000 amino acid. Molecular
weight (4000- 44000).
3. Shape: Globular (Insulin, enzymes), Oval (Albumin), Fibrous/Elongated (Fibrinogen).
4. Isoelectric pH: Protein exists as Zwitter ion or dipolar ion. The pH at which a protein has
equal number of positive and negative charges is known as isoelectric pH. When
subjected to an electric field the proteins do not move either towards anode or cathode,
hence this property is used to isolate proteins. The proteins become least soluble at
PROTEIN
Isoelectric pH and get precipitated. The Isoelectric pH of casein is 4.5 and at this pH the
casein in milk curdles producing the curd.
5. Precipitation of protein: By dehydration or neutralization.
6. Precipitation by salting out: Sodium sulphate and ammonium sulphate.
7. Precipitation by heavy metal: Pb2+, Hg2+, Fe2+ ,Zn2+, Cd2+.
8. Precipitation by anionic or alkaloidal reagent: Tannic acid, Trichloro acetic acid andsulphosalicylic acd etc.
9. Denaturation: Partial or complete unfolding (disorganization) of the native (natural)
protein structure is known as denaturation. This is caused by heat, acids, alkalies, alcohol,
acetone, urea, beta- mercaptoethanol.
10. Coagulation: When proteins are denatured by heat, they form insoluble aggregates known
as coagulum. All the proteins are not heat coagulable, only a few like the albumins,
globulins are heat coagulable.
CLASSIFICATION OF PROTEINS:
Proteins are classified based upon:
1. Solubility
2. Structural complexity
Classification based upon Solubility:
1. Fibrous proteins: These are insoluble in water. They include the structural proteins. They
have supportive function (e.g., collagen) and/or protective function (e.g., hair keratin and
fibrin).
2. Globular proteins: They are soluble in water. They include the functional proteins, e.g.,
enzymes, hemoglobin, etc.
Classification based upon Structural Complexity:
1. Simple
2. Conjugated
3. Derived proteins
1. Simple proteins: Proteins which are made up of amino acids only are known as simple
proteins.
They are further sub-divided into:
Example: Glutelin of wheat.
d. Prolamines:
Water insoluble but soluble in 70% alcohol,
They are water soluble, non-heat coagulable.
Example: Globin of haemoglobin.
h. Albuminoids or scleroproteins:
Insoluble in all neutral solvents, dilute acids or alkalis,
Example: keratin of hair and proteins of bone and cartilage.
2. Conjugated proteins: Proteins which are made up of amino acids and a non-amino
acid/protein substance called the prosthetic group are known as conjugated proteins.
The various types of conjugated proteins are:
a. Chromo proteins: The non-protein part is a colored compound in addition to the protein
part. Example: Haemoglobin has heme as the prosthetic group and cytochromes also have
heme.
a. Albumins:
They are water soluble, heat coagulable and are precipitated on full saturation with
ammonium sulphate,
Example: Serum albumin, lactalbumin and ovalbumin.
b. Globulins:
They are insoluble in water, but soluble in dilute salt solutions. They are heat
coagulable and precipitate on half-saturation with ammonium sulphate.
Example: erum globulin and ovo-globulin.
c. Glutelins:
They are insoluble in water and neutral solvents. Soluble in dilute acids and alkalis.
They are coagulated by heat,
Example: Gliadin of wheat, proteins of corn, barley, etc.
e. Histones:
Water soluble, basic in nature due to the presence of arginine and lysine, found in
nucleus. They help in DNA packaging in the cell. They form the protein moiety of
nucleoprotein.
f. Protamine’s:
Water soluble, basic in nature, not-heat coagulable. Found in sperm cells, hence
component of sperm nucleoprotein.
g. Globin’s:
b. Nucleoproteins:
These proteins are bound to nucleic acids.
Example: chromatin (histones + nucleic acids).
c. Glycoproteins: When a small amount of carbohydrate is attached to a protein it is known
as glycoproteins,
Example: mucin of saliva.
d. Phosphoprotein: Phosphoric acid is present with the protein.
Example: Milk casein and egg yolk (vitellin).
e. Lipoproteins: Proteins in combination with lipids,
Example: LDL, HDL.
f. Metalloproteins: They contain metal ion in addition to the amino acids,
Example: hemoglobin (iron), ceruloplasmin (copper).
3. Derived proteins: They are the proteins of low molecular weight produced from large
molecular weight proteins by the action of heat, enzymes or chemical agents.
Proteins → Proteans → Proteoses → Peptones → Peptides → Amino acids
Nutritional classification of protein:
1. Complete protein: Have all the ten essential amino acids. Promote good growth.
Example: Albumin (egg), Casein (Milk)
2. Partially complete protein: Partially lack one or more essential amino acid. Can
promote moderate growth.
Example: Wheat and rice protein (lack Lysine and threonine)
3. Incomplete protein: Completely lack one or more essential amino acid. Do not promote
growth.
Example: Gelatin (lack tryptophan), Zein (lack tryptophan, lysine)
BIOLOGICAL ROLE OF PROTEIN
1. Structural function
Structural protein: They give biological structure, strength or protection to the body tissue
system.
Example: Collagen, Gelatin, in bones and tendon, Elastin in ligaments and Keratin in
epidermal tissue (skin, hair, nails)
Contractile Proteins: Fibrous protein functioning in the contractile system of skeletal
muscles
Example: Myosin
2. Dynamic Function: Protein acting as enzyme, hormones, blood clotting factor,
immunoglobulin.
a. Enzymes : Highly specialized protein, catalyze most of the chemical reactions of organic
Biomolecules in cell, tissue and systems
Example: Pepsin, trypsin, hexokinase
b. Transport protein: Carry specific ions or molecules from one organ to another.
Example: Hemoglobin: carrier of oxygen and carbon dioxide.
Lipoprotein (Serum albumin): carrier of lipids from liver to the other organ.
Myoglobin (hemoglobin, serum albumin): Molecules and ions from one organ
to the other.
c. Nutrient and storage protein: They store and provide nutrients.
Example: Seed protein of wheat, corn and rice, albumin of egg white, casein of milk.
d. Defense protein: They defend (protect) the body from harmful foreign organisms,(bacteria, virus, foreign substance)
Example: Immunoglobulin’s
e. Regulatory protein: They help to regulate cellular or physiological activity,
Example: Hormones like insulin, Pituitary, parathyroid, growth hormones etc.
CLASSIFICATION OF PROTEIN
(Chemical nature & Composition)
SIMPLE PROTEINS CONJUGATED PROTEINS
Composed of only amino acid
residues
Albumins, Globulin
Glutelin, Histones,
Prolamines, Globin,
Lectins, Protamines
Globular proteins
Composed of prosthetic group (non
protein group) with amino acids
Chromoproteins
E.g. Haemoglobin
Prosthetic group is
carbohydrate
E.g. Mucin (saliva)
Other conjugated protein: Nucleoprotein, Mucoprotein, Lipoprotein, Metalloprotein
E.g. Casein (milk)
Collagens,
Elastins,
Keratins
Coagulated protein
Proteans
Metaproteins
Primary
Proteoses
Peptones
Polypeptides
Peptides
Denatured or degraded product of
hydrolysis of simple & conjugated protein
DERIVED PROTEINS
SecondaryScleroprotein
Prosthetic group is
Phosphoric acid
Prosthetic group is iron
pigments
Glycoproteins Phosphoproteins
CLASSIFICATION OF PROTEIN
(Physical nature)
FIBROUS PROTEINS GLOBULAR PROTEINS
Molecule is fiber shaped
Insoluble in water
Structural component of the body
E.g. Enzymes, Hormones, HaemoglobinE.g. Keratin, Myosin, Gelatin,
Collagen
Molecule is globular or spherical
Soluble in water
Regulation and maintenance of life process
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Amino acids are a group of organic compound contains two functional groups: Amino-
NH2 (Basic) and Carboxyl group-COOH (Acid).
Amino acids exist as Zwitterions ion in biological system. Chemically proteins are polymers of
L-α-amino acids. Amino acids are polymerized through formation of number of peptide linkages.
CLASSIFICATION OF AMINO ACID
On the basis of polarity:
1. Non polar amino acid - No charge on R group, hydrophobic (water hating). alanine,
leucine, isoleucine, valine, methionine, phenylalanine, tryptophan, proline.
2. Polar amino acid with no charge on R group: Glycine, serine, threonine, cysteine,
glutamine, asparginine, tyrosine.
AMINO ACIDS
On the basis of structure:
1.Amino acid with aliphatic side chain: Glycine,
alanine, valine, leucine and isoleucine
2.Hydroxyl group containing amino acid: Serine,
threonine, tyrosine
3.Sulfur containing amino acid- Cysteine, cystine,
methionine
4.Acidic amino acid and their amides: Aspartic
acid, asparginine, glutamic acid, glutamine
5.Basic amino acid: Lysine, arginine, histidine
6.Aromatic amino acid: Phenylalanine, tyrosine
and tryptophane
7.Imino acid: Proline
3. Polar amino acid with positive charge on R group: Lysine, arginine, histidine.
4. Polar amino acid with negative charge on R group: Glutamic acid, aspartic acid
On the basis of Nutritional requirement:
20 amino acids are required for the synthesis of variety of protein.
1. Essential Amino acids:
Amino acid cannot be synthesized by the body and need to be supplied from the diet is
called essential amino acid. The 10 essential amino acids are (A.V. HILL, MP, T.T.)
arginine, valine, histidine isoleucine leucine and lysine, methionine phenylalanine,
threonine, tryptophane. Arginine and histidine (semi essential amino acid, synthesized by
adult not by growing children).
2. Non Essential amino acids: The body can synthesize about 10 amino acids to meet the
biological need and need not to be consumed from the diet are called non essential amino
acid. Glycine, alanine, serine, tyrosine, cystine, asparginine, glutamic acid, glutamine,
aspartate, and proline.
On the basis of their metabolic fate:
1. Glycogenic amino acid: Serve as precursor for formation of glucose or glycogen.
Example: Alanine, aspartate, glycine, methionine.
2. Ketogenic amino acid: Amino acids which synthesize fat. Example: Leucine and Lysine
PROPERTIES OF AMINO ACID
Physical Properties of amino acid
1. Solubility: Usually soluble in water insoluble in organic solvent
2. Melting point: Melt at higher temperature.> 200oC
3. Taste: Sweet (Glycine, alanine, valine), Bitter( Arginine, Isoleucine), Tasteless( Leucine)
4. Optical properties : Except glycine
5. Ampholytes: Contain both acid and basic group. Donate proton and accept proton.
6. Zwitter ion or dipolar ion: Contain positive and negative ionic group
Chemical properties of amino acid:
1. Amino acid react with base to form salt (-COONa)
2. Amino acid react with alcohol to form ester (-COOR)
3. Decarboxylation: Produce corresponding amines
4. Amino acid reacts with ammonia to form Amide.
Aspartic acid + NH3 Asparginine
5. React with ninhydrin reagent gives purple (Ruhemann’s purple), blue or pink color
Amino acid + Ninhydrin Ketocaid + NH3 + CO2 + Hydrindantin
PurpleHydrindantin + NH3 + Ninhydrin
6. Transamination: Transfer of an amino acid group from an amino acid to a ketoacid to
form a new amino acid.
7. Oxidative deamination: Liberate ammonia